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Crystal structure of plant sesterterpene synthase AtTPS18
Structural highlights
FunctionPublication Abstract from PubMedClass I terpene synthase (TPS) generates bioactive terpenoids with diverse backbones. Sesterterpene synthase (sester-TPS, C25), a branch of class I TPSs, was recently identified in Brassicaceae. However, the catalytic mechanisms of sester-TPSs are not fully understood. Here, we first identified three nonclustered functional sester-TPSs (AtTPS06, AtTPS22, and AtTPS29) in Arabidopsis thaliana. AtTPS06 utilizes a type-B cyclization mechanism, whereas most other sester-TPSs produce various sesterterpene backbones via a type-A cyclization mechanism. We then determined the crystal structure of the AtTPS18-FSPP complex to explore the cyclization mechanism of plant sester-TPSs. We used structural comparisons and site-directed mutagenesis to further elucidate the mechanism: (1) mainly due to the outward shift of helix G, plant sester-TPSs have a larger catalytic pocket than do mono-, sesqui-, and di-TPSs to accommodate GFPP; (2) type-A sester-TPSs have more aromatic residues (five or six) in their catalytic pocket than classic TPSs (two or three), which also determines whether the type-A or type-B cyclization mechanism is active; and (3) the other residues responsible for product fidelity are determined by interconversion of AtTPS18 and its close homologs. Altogether, this study improves our understanding of the catalytic mechanism of plant sester-TPS, which ultimately enables the rational engineering of sesterterpenoids for future applications. Molecular Basis for Sesterterpene Diversity Produced by Plant Terpene Synthases.,Chen Q, Li J, Liu Z, Mitsuhashi T, Zhang Y, Liu H, Ma Y, He J, Shinada T, Sato T, Wang Y, Liu H, Abe I, Zhang P, Wang G Plant Commun. 2020 Apr 29;1(5):100051. doi: 10.1016/j.xplc.2020.100051., eCollection 2020 Sep 14. PMID:33367256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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